| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NQO2 |
| Uniprot No | P16083 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-231aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q |
| 预测分子量 | 28 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于NQO2重组蛋白的3篇参考文献示例(文献名称与作者为虚构，仅供示例参考)：
1. **"Recombinant Expression and Functional Characterization of Human NQO2 in Escherichia coli"**
- **作者**: Smith A, et al.
- **摘要**: 本研究成功在大肠杆菌中重组表达了人源NQO2蛋白，并通过亲和层析纯化获得高纯度蛋白。酶动力学分析表明，重组NQO2对底物双氢生物蝶呤(dihydrobiopterin)具有显著催化活性，且其活性依赖锌离子的辅助。
2. **"Structural Insights into the Catalytic Mechanism of NQO2 via X-ray Crystallography"**
- **作者**: Zhang Y, et al.
- **摘要**: 通过X射线晶体学解析了重组NQO2蛋白的三维结构(分辨率2.1 Å)，揭示了其与辅因子黄素单核苷酸(FMN)的结合位点及底物识别区域，为开发靶向NQO2的抑制剂提供了结构基础。
3. **"Role of NQO2 in Cellular Redox Regulation: Implications in Neurodegenerative Diseases"**
- **作者**: Wang L, et al.
- **摘要**: 利用重组NQO2蛋白研究其在细胞氧化应激中的作用，发现NQO2通过调节醌类化合物的代谢影响神经细胞活性，提示其可能在帕金森病等神经退行性疾病中起关键作用。
(注：以上文献为模拟内容，实际研究中请通过PubMed、Web of Science等平台检索真实文献。)
NAD(P)H:quinone oxidoreductase 2 (NQO2), also known as quinone reductase 2. is a flavoprotein enzyme encoded by the NQO2 gene in humans. It belongs to the quinone oxidoreductase family, sharing structural homology with NQO1 but exhibiting distinct functional characteristics. Unlike NQO1. which utilizes FAD as a cofactor and NADH/NADPH as electron donors, NQO2 preferentially employs dihydrobiopterin (BH2) as its cofactor and NRH (reduced β-nicotinamide riboside) as an electron donor. This unique cofactor specificity differentiates its catalytic mechanism and biological roles.
NQO2 is ubiquitously expressed in human tissues, with higher levels observed in the liver, kidney, and brain. It participates in cellular detoxification by catalyzing the two-electron reduction of quinones and related compounds, preventing the formation of harmful semiquinone radicals. This antioxidant function links NQO2 to oxidative stress regulation and potential roles in neurodegenerative diseases and cancer. Notably, NQO2 demonstrates both tumor-suppressive and oncogenic activities depending on cellular context, interacting with various cancer-related proteins such as p53 and HIF-1α.
Recombinant NQO2 protein, typically produced in Escherichia coli or mammalian expression systems, enables detailed study of its structure-function relationships. Structural analyses reveal a homotetrameric configuration with distinct substrate-binding pockets, providing insights for drug development. The enzyme's ability to metabolize certain chemotherapeutic agents and environmental toxins has spurred interest in its pharmacological applications. Additionally, NQO2 polymorphisms have been associated with altered disease susceptibility, emphasizing its clinical relevance. Current research focuses on elucidating its role in neurodegenerative pathologies like Alzheimer's disease, where it may influence tau protein aggregation and neuronal apoptosis. As a multifunctional enzyme, NQO2 continues to be a compelling subject for investigating cellular redox biology and therapeutic targeting.
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